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Information on EC 2.3.1.168 - dihydrolipoyllysine-residue (2-methylpropanoyl)transferase and Organism(s) Homo sapiens
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2.3.1.168 dihydrolipoyllysine-residue (2-methylpropanoyl)transferaseIUBMB Comments
A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
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Word Map
- 2.3.1.168
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branched-chain
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bcaas
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merits
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protein-restricted
- retinal
- urine
- metformin
- women
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maple
- l-glutamate
- syrup
- agriculture
- synthesis
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dihydrolipoamide branched chain transacylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dihydrolipoyl transacetylase
E2p
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E2p is a component of the human multienzyme pyruvate dehydrogenase complex
additional information
dihydrolipoyl transacetylase
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-
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dihydrolipoyl transacetylase
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enzyme is the E2 component of the human pyruvate dehydrogenase complex
additional information
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enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
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enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
additional information
enzyme is the E2 component of the multienzyme complex branched-chain alpha-keto acid dehydrogenase, i.e. branched-chain 2-oxo acid dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkyl group transfer
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase
A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
additional information
?
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enzyme is a mitochondrial autoantigen, epitope mapping is performed to define the recognition sites by sera and T cells of patients suffering idopathic dilated cardiomyopathy and dilated cardiomyopathy
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-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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-
?
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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enzyme contains 1 lipoyl residue per E2 chain of branched-chain 2-oxo acid dehydrogenase
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?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
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part of the pyruvate dehydrogenase reaction
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?
acetyl-CoA + dihydrolipoamide
CoA + S-acetyldihydrolipoamide
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enzyme contains 2 lipoyl residues per E2 chain of pyruvate dehydrogenase complex
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine
CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
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?
additional information
?
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enzyme is a mitochondrial autoantigen, epitope mapping is performed to define the recognition sites by sera and T cells of patients suffering idopathic dilated cardiomyopathy and dilated cardiomyopathy
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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inhibition tests of the multienzyme complex with sera from patients suffering the possibly autoimmune diseases idopathic dilated cardiomyopathy and dilated cardiomyopathy to perform epitope mapping, overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
branched-chain amino acids are metabolized within both the vasculature and neurons in the human brain. Glutamate dehydrogenase isozymes, branched-chain aminotransferase and the branched-chain alpha-ketoacid dehydrogenase proteins may operate in conjunction with astrocytic glutamate transporters and glutamine synthetase to regulate the availability of glutamate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ODB2_HUMAN
482
0
53487
Swiss-Prot
Mitochondrion (Reliability: 1)
DLDH_HUMAN
509
0
54177
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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lipoyl domains and inner core in the structure of multienzyme complex, overview
additional information
assembly of 24 E2 subunits into a cubic structure, forming the core of the mammalian branched-chain alpha-keto acid dehydrogenase multienzyme complex
additional information
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The human pyruvate dehydrogenase complex (PDC) is organized around a 60-meric dodecahedral core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding protein (E3BP), which specifically tethers E3 dimers to the PDC. Using an in vitro reconstituted PDC, densitometry, isothermal titration calorimetry, and analytical ultracentrifugation evidence provide that there are 40 copies of E2p and 20 copies of E3BP in the E2p/E3BP core. The overall maximal stoichiometry of this in vitro assembled PDC for E2p:E3BP:E1p:E3 is 40:20:40:20.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F214C
natural splicing mutant from WG-34 cells, related to the maple syrup urine disease, phenotype of homo- and heterozygous mutations in humans
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant E2 fusion protein from Escherichia coli, the tag is cleaved off by factor Xa
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of full length E2 and fragments, expression in Escherichia coli JM109 as fusion protein
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pseudogene E2, DNA sequence determination and analysis, retroposon, gene corresponds to the complete mitochondrial presequence and the lipoyl-bearing domain encoded by exon I through IV of the functional gene E2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chuang, D.T.; Fisher, C.W.; Lau, K.S.; Griffin, T.A.; Wynn, R.M.; Cox, R.P.
Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex
Mol. Biol. Med.
8
49-63
1991
Bos taurus, Homo sapiens (P11182)
Lau, K.S.; Herring, W.J.; Chuang, J.L.; McKean, M.; Danner, D.J.; Cox, R.P.; Chuang, D.T.
Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene
J. Biol. Chem.
267
24090-24096
1992
Homo sapiens (P11182)
Lau, K.S.; Chuang, J.L.; Herring, W.J.; Danner, D.J.; Cox, R.P.; Chuang, D.T.
The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex
Biochim. Biophys. Acta
1132
319-321
1992
Homo sapiens (P11182)
Ansari, A.A.; Neckelmann, N.; Villinger, F.; Leung, P.; Danner, D.J.; Brar, S.S.; Zhao, S.; Gravanis, M.B.; Mayne, A.; Gershwin, M.E.
Epitope mapping of the branched chain alpha-ketoacid dehydrogenase dihydrolipoyl transacylase (BCKD-E2) protein that reacts with sera from patients with idiopathic dilated cardiomyopathy
J. Immunol.
153
4754-4765
1994
Bos taurus, Homo sapiens
Perham, R.N.
Swinging arms and swinging domains in multifunctional emzymes: catalytic machines for multistep reactions
Annu. Rev. Biochem.
69
961-1004
2000
Acidithiobacillus ferrooxidans, Azotobacter vinelandii, Cupriavidus necator, Enterococcus faecalis, Escherichia coli, Geobacillus stearothermophilus, Haemophilus influenzae, Homo sapiens, Neisseria meningitidis, no activity in archaebacteria, no activity in Desulfovibrio africanus, Saccharomyces cerevisiae, Zymomonas mobilis
Brautigam, C.A.; Wynn, R.M.; Chuang, J.L.; Chuang, D.T.
Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex
J. Biol. Chem.
284
13086-13098
2009
Homo sapiens
Hull, J.; Usmari Moraes, M.; Brookes, E.; Love, S.; Conway, M.
Distribution of the branched-chain alpha-ketoacid dehydrogenase complex E1alpha subunit and glutamate dehydrogenase in the human brain and their role in neuro-metabolism
Neurochem. Int.
112
49-58
2018
Homo sapiens (P09622)
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